Activity of purified hepatitis C virus protease NS3 on peptide substrates
about
Selection of functional variants of the NS3-NS4A protease of hepatitis C virus by using chimeric sindbis virusesMultiple enzymatic activities associated with recombinant NS3 protein of hepatitis C virusIn vivo selection of protease cleavage sites by using chimeric Sindbis virus librariesComplete translation of the hepatitis C virus genome in vitro: membranes play a critical role in the maturation of all virus proteins except for NS3.Virus-specific cofactor requirement and chimeric hepatitis C virus/GB virus B nonstructural protein 3Isolation and characterization of monoclonal antibodies that inhibit hepatitis C virus NS3 proteaseChimeric Sindbis viruses dependent on the NS3 protease of hepatitis C virusPolynucleotide modulation of the protease, nucleoside triphosphatase, and helicase activities of a hepatitis C virus NS3-NS4A complex isolated from transfected COS cellsGB virus B and hepatitis C virus NS3 serine proteases share substrate specificityBovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replicationProbing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptidesIn vitro study of the NS2-3 protease of hepatitis C virusCharacterization of engineered hepatitis C virus NS3 protease inhibitors affinity selected from human pancreatic secretory trypsin inhibitor and minibody repertoiresConformational changes in the NS3 protease from hepatitis C virus strain Bk monitored by limited proteolysis and mass spectrometryKinetic, Mutational, and Structural Studies of the Venezuelan Equine Encephalitis Virus Nonstructural Protein 2 Cysteine ProteaseNew details of HCV NS3/4A proteinase functionality revealed by a high-throughput cleavage assayA highly scalable peptide-based assay system for proteomicsImmune evasion by hepatitis C virus NS3/4A protease-mediated cleavage of the Toll-like receptor 3 adaptor protein TRIFEngineered toxins "zymoxins" are activated by the HCV NS3 protease by removal of an inhibitory protein domain.Increasing rate of cleavage at boundary between non-structural proteins 4B and 5A inhibits replication of hepatitis C virus.The NS4A Cofactor Dependent Enhancement of HCV NS3 Protease Activity Correlates with a 4D Geometrical Measure of the Catalytic Triad Region.Establishment of a cell-based assay system for hepatitis C virus serine protease and its primary applications.Conserved C-terminal threonine of hepatitis C virus NS3 regulates autoproteolysis and prevents product inhibition.Identification of residues in the dengue virus type 2 NS2B cofactor that are critical for NS3 protease activation.The effect of prime-site occupancy on the hepatitis C virus NS3 protease structure.The Discovery and Development of Boceprevir: A Novel, First-generation Inhibitor of the Hepatitis C Virus NS3/4A Serine Protease.Protease inhibitors as antiviral agents.
P2860
Q27469337-8811ABB5-6662-4BDF-9B9A-3433210E4910Q27469559-F7B30F3B-9762-4823-A9A5-D7A6E3B5F660Q27469601-96EB5B70-91AE-4ADE-9EC7-771F54EC072CQ27469609-F23D0D99-72AB-40D8-A6DA-E3727D4456F5Q27469660-66021CC8-9E75-49E4-BC07-B83FB2073CD6Q27469674-1E0B3904-120D-44BB-B32D-F54F923B13C9Q27480780-ECE626C9-037B-4256-B712-59BFB83DC0C3Q27480818-60C495BA-F11F-40C2-B9ED-EF195194BE44Q27480829-E9D07E43-7991-4A86-8796-BCCB53784697Q27480836-655C87A0-0439-4FD9-B094-63F1D3E8D776Q27480843-B88EB1C4-3E05-45A9-8E03-0D93188B2C8FQ27480845-44645217-A30F-47A5-B73B-1424E3F3D4DDQ27480876-301E27BC-D18D-4DF8-A42F-54E60C41412DQ27484276-6A9F288F-E618-48C7-A34D-7CC17C344B6CQ27704471-6AAA62F8-2210-41D9-AFB2-F8FFF3FC5CA2Q28482890-668FD0CA-D48E-4DC0-BBD8-A2E068742CC0Q28728598-74ACC8E2-5349-4E4B-BE2D-B25CD8A4153AQ29547901-ECA69DEE-568E-4600-BC04-86574E611DC6Q33802605-69034128-9582-457D-ABB1-09FDE8347FA8Q34074690-A26821B2-6BAA-4A1E-9D4E-5880F906D1D5Q36218266-D0534679-2D5A-4CF1-9D9E-5DAF45179F34Q36308835-1E36D3E5-2141-4323-BC2D-D72FA987C184Q36942703-FE992F5E-C4EE-446C-BE26-F138F2453D55Q37682862-25A36CE9-16DA-4D98-840A-D7C81E629F6BQ38269787-E913119B-AB84-4495-AA65-FD104743A8DAQ38584274-623A3592-CA0D-447E-BD41-5386361E0CC0Q39468942-AEC41B07-14DC-4656-B4E5-F73447ED2650
P2860
Activity of purified hepatitis C virus protease NS3 on peptide substrates
description
1996 nî lūn-bûn
@nan
1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@ast
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@en
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@nl
type
label
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@ast
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@en
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@nl
prefLabel
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@ast
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@en
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@nl
P2093
P2860
P1433
P1476
Activity of purified hepatitis C virus protease NS3 on peptide substrates
@en
P2093
Steinkühler C
P2860
P304
P577
1996-10-01T00:00:00Z